ID A0A060S2I6_PYCCI Unreviewed; 827 AA.
AC A0A060S2I6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Extracellular metalloproteinase {ECO:0000256|RuleBase:RU364017};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU364017};
DE AltName: Full=Fungalysin {ECO:0000256|RuleBase:RU364017};
GN ORFNames=BN946_scf184998.g17 {ECO:0000313|EMBL:CDO68520.1};
OS Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Trametes.
OX NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO68520.1, ECO:0000313|Proteomes:UP000029665};
RN [1] {ECO:0000313|EMBL:CDO68520.1, ECO:0000313|Proteomes:UP000029665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM137 {ECO:0000313|EMBL:CDO68520.1,
RC ECO:0000313|Proteomes:UP000029665};
RA Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA Pontarotti P., Henrissat B., Record E.;
RT "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT breakdown.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601842-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601842-2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU364017}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family.
CC {ECO:0000256|ARBA:ARBA00006006, ECO:0000256|RuleBase:RU364017}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO68520.1}.
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DR EMBL; CCBP010000020; CDO68520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060S2I6; -.
DR HOGENOM; CLU_012703_3_2_1; -.
DR OMA; IRKDSYT; -.
DR OrthoDB; 2786251at2759; -.
DR Proteomes; UP000029665; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364017};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601842-2,
KW ECO:0000256|RuleBase:RU364017};
KW Metalloprotease {ECO:0000256|RuleBase:RU364017};
KW Protease {ECO:0000256|RuleBase:RU364017};
KW Reference proteome {ECO:0000313|Proteomes:UP000029665};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364017};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364017};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601842-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|RuleBase:RU364017}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT CHAIN 20..827
FT /note="Extracellular metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU364017"
FT /id="PRO_5009359629"
FT DOMAIN 78..128
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT REGION 773..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 551
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ SEQUENCE 827 AA; 91745 MW; 94C81076ACDE678A CRC64;
MRRLFVAALA AAGLAGVLAH DSHQVSRRKT LGFGPVLPNA AYHTNPVYHT SLLRASSDPF
EVARVFVKDL VRGIPGSDFV IRKDSYTDEA TGVTHVYVRQ YVNGIEVADG DINVNIKDGV
VLSYGDSFFR PKDSTDMFTA ASSSSDPHSE YCQSLETEIA NQLQHLDVHK TGERSNALEQ
LAYLYEWNCK FVDAPEFLAD HPDFAAAEDA ASGDISRALL QFMLAATPNA ELQAQILDNP
KKFIPEMRVS FQHHHHTDQP FFTVENVPDT VNPVKGRLAF VQVPQGDSTT LQLVYKFEVE
MQDNWYETAV SAEMPHRIIS VVDWANDSPV PLAPVPKEPQ SATYRVFEWG INDPSLGDRS
IQKENFDALA SPWGWHALPV ANDPSSSYLS AKDASKIRNT TTTWGNNVFA HEDWEGRNNW
VNNYRPDAGP RKAFDFVYQP KKTDSEDALE EAQKYINATV TQLFYTSNLV HDLYYRYGFH
ELAGNFQQYN FGRGGEENDA VIANAQDGSG YNNANFMTPP DGQNGRCRMY LWNTANPYRD
GDLEAGIVIH ELAHGLSIRL TGGPANSGCL GWGESGGMGE GWGDFLATTI RSNKNYSDYA
MGSWAANMEK GIRNYPYSLN QTINPSTYAT LDKPGYWGVH AIGEVWAQIL WVVSQKLIEK
HGFTEDLFPP KPLEDGTIPE GDFYRKAEYT SDGKRKPLVP KHGNSLMVQL VLNGMKLQPC
RPSFFDARDA IIAADKTLTG GENFCDLWQG FASRGLGVDA AVKGRTPWGG GVRSNGYAVP
AECQNGDVPP PADPAPGDGD DDGDDDDWPW LQWVVEKTTV FSWSWPL
//
